Studies indicate that there is a structural and functional relationship in the mechanism by which glycoprotein hormones (thyrotropin (TSH), luteinizing hormone (LH), human chorionic gonadotropin (hCG), and follicle-stimulating hormone (FSH), certain bacterial toxins (cholera and tetanus, for example), and the antiviral protective agent, interferon, transmit their message through the cell membrane. Thus, in each case these agents appear to be composed of two subunits or regions in their molecular structure, i.e., the alpha and beta subunits of the glycoprotein hormones or the A and B proteins of cholera toxin. One subunit or region, the Beta subunit or B protein of the hormones and cholera toxin, for example, interacts with a receptor containing a ganglioside or ganglioside-like molecule whose oligosaccharide determinant causes a specific conformational change in the hormone molecule; interaction with a receptor containing the wrong oligosaccharide moiety will not cause this conformational change and will therefore not allow further message transmission. As a consequence of the initial interaction. BIBLIOGRAPHIC REFERENCES: Aloj, S.M., and Ingham, K.C.: Kinetics of subunit interactions in glyco-protein hormones. In James, V.H.T.(ed.): Proceedings of the 5th International Congress of Endocrinology, Hamburg, July 18-24, 1976. International Congress Series No. 403, Amsterdam, The Netherlands, Excerpta Medica, pp. 108-113, Vol. 2, 1977. Aloj, S.M., Kohn, L.D., Lee, G., and Meldolesi, M.F.: The binding of thyrotropin to liposomes containing gangliosides. Biochem. Biophys. Res. Commun. 74: 1053-1059, 1977.